1mf6: Difference between revisions

Line 1:

[[~~Image~~:1mf6.~~png|left|200px~~]]

==Transducin gamma subunit, C-terminal domain 60-71, rhodopsin-bound state: Ensemble of 15 models determined by TrNOE spectroscopy==

== Structural highlights ==

<table><tr><td colspan='2'>[[1mf6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MF6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MF6 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mf6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mf6 RCSB], [http://www.ebi.ac.uk/pdbsum/1mf6 PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

Rhodopsin, a prototypical G protein-coupled receptor, catalyzes the activation of a heterotrimeric G protein, transducin, to initiate a visual signaling cascade in photoreceptor cells. The betagamma subunit complex, especially the C-terminal domain of the transducin gamma subunit, Gtgamma(60-71)farnesyl, plays a pivotal role in allosteric regulation of nucleotide exchange on the transducin alpha subunit by light-activated rhodopsin. We report that this domain is unstructured in the presence of an inactive receptor but forms an amphipathic helix upon rhodopsin activation. A K65E/E66K charge reversal mutant of the gamma subunit has diminished interactions with the receptor and fails to adopt the helical conformation. The identification of this conformational switch provides a mechanism for active GPCR utilization of the betagamma complex in signal transfer to G proteins.

~~{{STRUCTURE_1mf6| PDB=1mf6 | SCENE= }}~~

Rhodopsin controls a conformational switch on the transducin gamma subunit.,Kisselev OG, Downs MA Structure. 2003 Apr;11(4):367-73. PMID:12679015<ref>PMID:12679015</ref>

~~===Transducin gamma subunit~~, ~~C-terminal domain 60-71, rhodopsin-bound state: Ensemble~~ of ~~15 models determined by TrNOE spectroscopy===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_12679015}}~~

== References ==

==~~About this Structure~~==

__TOC__

~~[[1mf6]] is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MF6 OCA].~~

</StructureSection>

[[Category: Bos taurus]]

[[Category: Kisselev, O G.]]

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@@ Line 1: / Line 1: @@
-[[Image:1mf6.png|left|200px]]
+==Transducin gamma subunit, C-terminal domain 60-71, rhodopsin-bound state: Ensemble of 15 models determined by TrNOE spectroscopy==
+<StructureSection load='1mf6' size='340' side='right' caption='[[1mf6]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1mf6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MF6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MF6 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mf6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mf6 RCSB], [http://www.ebi.ac.uk/pdbsum/1mf6 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Rhodopsin, a prototypical G protein-coupled receptor, catalyzes the activation of a heterotrimeric G protein, transducin, to initiate a visual signaling cascade in photoreceptor cells. The betagamma subunit complex, especially the C-terminal domain of the transducin gamma subunit, Gtgamma(60-71)farnesyl, plays a pivotal role in allosteric regulation of nucleotide exchange on the transducin alpha subunit by light-activated rhodopsin. We report that this domain is unstructured in the presence of an inactive receptor but forms an amphipathic helix upon rhodopsin activation. A K65E/E66K charge reversal mutant of the gamma subunit has diminished interactions with the receptor and fails to adopt the helical conformation. The identification of this conformational switch provides a mechanism for active GPCR utilization of the betagamma complex in signal transfer to G proteins.
-{{STRUCTURE_1mf6|  PDB=1mf6  |  SCENE=  }}
+Rhodopsin controls a conformational switch on the transducin gamma subunit.,Kisselev OG, Downs MA Structure. 2003 Apr;11(4):367-73. PMID:12679015<ref>PMID:12679015</ref>
-===Transducin gamma subunit, C-terminal domain 60-71, rhodopsin-bound state: Ensemble of 15 models determined by TrNOE spectroscopy===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_12679015}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[1mf6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MF6 OCA].
+</StructureSection>
 [[Category: Bos taurus]]
 [[Category: Kisselev, O G.]]